Yeast Pab1 Interacts with Rna15 and Participates in the Control of the Poly(A) Tail Length In Vitro

Amrani, Nadia; Minét, Michèle; Gouar, Martine Le; Lacroute, François; Wyers, Françoise

doi:10.1128/mcb.17.7.3694

Cited by 131 publications

(158 citation statements)

References 43 publications

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“…Consistent with this view, decapping becomes independent of poly(A) in mutant strains that lack Pab1p, such that mRNAs with long poly(A) tails are decapped (Caponigro and Parker 1995). The effects of pab1 mutations on cellular mRNA levels may be complex, with contributions from turnover and/ or nuclear processes, such as mRNA 3Ј-end formation (Caponigro and Parker 1995;Amrani et al 1997;Keller and Minvielle-Sebastia 1997;Minvielle-Sebastia et al 1997;J. Morrisey and A. Sachs, pers.…”

mentioning

confidence: 49%

mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation

1998

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Translation and mRNA stability are enhanced by the presence of a poly(A) tail. In vivo, the tail interacts with a conserved polypeptide, poly(A) binding protein (Pab1p). To examine Pab1p function in vivo, we have tethered Pab1p to the 3 UTR of reporter mRNAs by fusing it to MS2 coat protein and placing MS2 binding sites in the 3 UTR of the reporter. This strategy allows us to uncouple Pab1p function from its RNA binding activity. We show that mRNAs that lack a poly(A) tail in vivo are stabilized by Pab1p, and that the portions of Pab1p required for stabilization are genetically distinct from those required for poly(A) binding. In addition, stabilization by Pab1p requires ongoing translation of the mRNA. We conclude that the primary, or sole, function of poly(A) with respect to mRNA stability is simply to bring Pab1p to the mRNA, and that mRNA stabilization is an intrinsic property of Pab1p. The approach we describe may be useful in identifying and assaying 3 UTR regulatory proteins, as it uncouples analysis of function from RNA binding.

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confidence: 49%

mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation

1998

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“…The polyadenylation reaction can occur without PABP, but controlling the length of the poly(A) tail requires PABP [192][193][194][195]. PABP binds directly to nascent stretches of 11-14 adenylate nucleotides as they become available [196], and this binding continues until the proper poly(A) tail length is reached (~200 to 300 bases in mammals) [197].…”

Section: Poly(a) Binding Proteinmentioning

confidence: 99%

“…In addition, direct binding of PABP to premRNA, adjacent to PAP, increases the efficiency of polyadenylation 80-fold [198]. Pab1p binds directly to Rna15p, which possibly recruits Pab1p to the polyadenylation site [192]. Interactions between PABP and other members of the mammalian 3′-end processing complex have not been reported.…”

Section: Poly(a) Binding Proteinmentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

364

482

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Most eukaryotic mRNA precursors (pre-mRNAs) must undergo extensive processing, including cleavage and polyadenylation at the 3′-end. Processing at the 3′-end is controlled by sequence elements in the pre-mRNA (cis elements) as well as protein factors. Despite the seeming biochemical simplicity of the processing reactions, more than 14 proteins have been identified for the mammalian complex, and more than 20 proteins have been identified for the yeast complex. The 3′-end processing machinery also has important roles in transcription and splicing. The mammalian machinery contains several sub-complexes, including cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF), cleavage factor I (CF I m ), and cleavage factor II (CF II m ). Additional protein factors include poly(A) polymerase (PAP), poly(A) binding protein (PABP), symplekin, and the C-terminal domain (CTD) of RNA polymerase II largest subunit. The yeast machinery includes cleavage factor IA (CF IA), cleavage factor IB (CF IB), and cleavage and polyadenylation factor (CPF).

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“…Functional studies in a wide variety of organisms ranging from yeast to humans have demonstrated that members of this evolutionarily conserved protein family (reviewed in refs. 7-9) directly contact the poly(A) tail of mRNA transcripts to regulate transcript polyadenylation (10,11), translation (12)(13)(14)(15)(16), stability (17,18), and possibly nuclear export (19,20). All known Pab family members specifically bind to poly(A) RNA via at least one RNA recognition motif (RRM) (21,22).…”

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confidence: 99%

Recognition of polyadenosine RNA by zinc finger proteins

Kelly¹,

Pabit

Kitchen

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

124

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Messenger RNA transcripts are coated from cap to tail with a dynamic combination of RNA binding proteins that process, package, and ultimately regulate the fate of mature transcripts. One class of RNA binding proteins essential for multiple aspects of mRNA metabolism consists of the poly(A) binding proteins. Previous studies have concentrated on the canonical RNA recognition motif-containing poly(A) binding proteins as the sole family of poly(A)-specific RNA binding proteins. In this study, we present evidence for a previously uncharacterized poly(A) recognition motif consisting of tandem CCCH zinc fingers. We have probed the nucleic acid binding properties of a yeast protein, Nab2, that contains this zinc finger motif. Results of this study reveal that the seven tandem CCCH zinc fingers of Nab2 specifically bind to polyadenosine RNA with high affinity. Furthermore, we demonstrate that a human protein, ZC3H14, which contains CCCH zinc fingers homologous to those found in Nab2, also specifically binds polyadenosine RNA. Thus, we propose that these proteins are members of an evolutionarily conserved family of poly(A) RNA binding proteins that recognize poly(A) RNA through a fundamentally different mechanism than previously characterized RNA recognition motif-containing poly(A) binding proteins.CCCH zinc finger ͉ poly(A) binding protein ͉ RNA binding

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Yeast Pab1 Interacts with Rna15 and Participates in the Control of the Poly(A) Tail Length In Vitro

Cited by 131 publications

References 43 publications

mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation

mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation

Protein factors in pre-mRNA 3′-end processing

Recognition of polyadenosine RNA by zinc finger proteins

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